R1003
Ribonuclease T1 from Aspergillus oryzae
ammonium sulfate suspension, 300,000-600,000 units/mg protein
Synonym(s):
Guanyloribonuclease, Ribonucleate 3′-guanylo-oligonucleotidohydrolase
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-809-1
MDL number:
Specific activity:
300,000-600,000 units/mg protein
Biological source:
Aspergillus sp. (Aspergillus oryzae)
biological source
Aspergillus sp. (Aspergillus oryzae)
Quality Level
form
ammonium sulfate suspension
specific activity
300,000-600,000 units/mg protein
mol wt
11068 by amino acid sequence
technique(s)
cell based assay: suitable
suitability
suitable for separating native or denatured proteins, or nucleic acids
application(s)
cell analysis
storage temp.
2-8°C
Application
Ribonuclease T1 (RNase T1) from Aspergillus oryzae is used to digest denatured RNA prior to sequencing and is used for protein folding studies .
Biochem/physiol Actions
Ribonuclease T1 (RNase T1) from Aspergillus oryzae is an endoribonuclease that hydrolyzes after G residues. Cleavage occurs between the 3′-phosphate group of a guanidine ribonucleotide and 5′-hydroxyl of the adjacent nucleotide. The initial product is a 2′:3′ cyclic phosphate nucleoside that is hydrolyzed to the corresponding 3′-nucleoside phosphate. It differs from Pancreatic RNase in that it attacks the guanine sites specifically to yield 3′-GMP and oligonucleotides with a 3′-GMP terminal group.
Physical form
Suspension in 2.8 M (NH4)2SO4 solution
Analysis Note
Protein determined by E1%/280
Other Notes
One unit will produce acid soluble oligonucleotides equivalent to a ΔA260 of 1.0 in 15 min at pH 7.5 at 37°C, in a reaction volume of 1.0 mL. Substrate: Yeast RNA.
Storage Class
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves
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Product Information Sheet
Ribonuclease T1: Structure, Function, and Stability
Pace, CN; Heinemann U, et al.
Angewandte Chemie (International Edition in English), 4, 343-360 (1991)
C Nick Pace et al.
Journal of molecular biology, 408(3), 514-528 (2011-03-08)
Our goal was to gain a better understanding of the contribution of hydrophobic interactions to protein stability. We measured the change in conformational stability, Δ(ΔG), for hydrophobic mutants of four proteins: villin headpiece subdomain (VHP) with 36 residues, a surface
S Dubey et al.
Journal of controlled release : official journal of the Controlled Release Society, 152(3), 356-362 (2011-03-15)
Cathodal iontophoresis of anionic macromolecules has been considered a major challenge owing to (i) the presence of a negative charge on the skin under physiological conditions and (ii) the electroosmotic solvent flow in the (opposite) anode-to-cathode direction. Moreover, electroosmosis, and